

@article {3743,
	title = {Mechanism for coordinated \{\{\}{RNA}\{\}\} packaging and genome replication by rotavirus polymerase \{\{\}{VP}1.\{\}\}},
	journal = {Structure \{\{\}(London,\{\}\} England : 1993)},
	volume = {16},
	number = {11},
	year = {2008},
	pages = {1678{\textendash}1688},
	abstract = {Rotavirus \{\{\}RNA-dependent\{\}\} \{\{\}RNA\{\}\} polymerase \{\{\}VP1\{\}\} catalyzes \{\{\}RNA\{\}\} synthesis within a subviral particle. This activity depends on core shell protein \{\{\}VP2.\{\}\} A conserved sequence at the 3\{\{\}\${\textbackslash}backslash\$textquoteright\{\}\} end of plus-strand \{\{\}RNA\{\}\} templates is important for polymerase association and genome replication. We have determined the structure of \{\{\}VP1\{\}\} at 2.9 A resolution, as apoenzyme and in complex with \{\{\}RNA.\{\}\} The cage-like enzyme is similar to reovirus lambda3, with four tunnels leading to or from a central, catalytic cavity. A distinguishing characteristic of \{\{\}VP1\{\}\} is specific recognition, by conserved features of the template-entry channel, of four bases, \{\{\}UGUG,\{\}\} in the conserved 3\{\{\}\${\textbackslash}backslash\$textquoteright\{\}\} sequence. Well-defined interactions with these bases position the \{\{\}RNA\{\}\} so that its 3\{\{\}\${\textbackslash}backslash\$textquoteright\{\}\} end overshoots the initiating register, producing a stable but catalytically inactive complex. We propose that specific 3\{\{\}\${\textbackslash}backslash\$textquoteright\{\}\} end recognition selects rotavirus \{\{\}RNA\{\}\} for packaging and that \{\{\}VP2\{\}\} activates the autoinhibited \{\{\}VP1/RNA\{\}\} complex to coordinate packaging and genome replication.},
	doi = {10.1016/j.str.2008.09.006},
	url = {http://dx.doi.org/10.1016/j.str.2008.09.006},
	author = {Lu, Xiaohui and McDonald, Sarah M and Tortorici, M A and Tao, Yizhi J and Vasquez-Del Carpio, Rodrigo and Nibert, Max L and Patton, John T and Harrison, Stephen C}
}
